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activated blood-coagulation factor X
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-
-
-
activated Stuart-Prower factor
-
-
-
-
autoprothrombin C
-
-
-
-
blood coagulation factor X
zymogen
blood coagulation factor Xa
blood-coagulation factor X, activated
-
-
-
-
plasma thromboplastin
-
-
-
-
procoagulant factor X
-
-
thromboplastin, plasma
-
-
-
-
Trocarin prothrombin activator
-
-
-
-
Virus activating protease
-
-
-
-
activated factor X
-
-
-
-
blood coagulation factor Xa
-
-
blood coagulation factor Xa
-
clotting factor Xa
-
-
coagulation factor Xa
-
-
-
-
coagulation factor Xa
-
-
coagulation factor Xa
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-
coagulation factor Xa
-
-
coagulation factor Xa
-
-
coagulation factor Xa
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-
factor X
-
-
factor Xa
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-
-
-
factor Xa
-
mature enzyme
factor Xa
-
-
649797, 649955, 650111, 650170, 650179, 650193, 650336, 650463, 650846, 650914, 650933, 650938, 650939, 651189, 652253, 652262, 652278, 652349, 652447, 652728, 652731, 652755, 653979, 664120, 683178, 683235, 683252, 683629, 683823, 707025, 707279, 707307, 707693, 707903, 708249, 708321, 708322, 708509, 708634, 708815, 709156, 709211, 709434, 709578, 709726, 709729, 710601, 710607, 717234, 717253, 717336, 717381, 717829, 717968, 717974, 731276, 731308, 731484, 731588, 731756, 731958, 732376, 732937, 752707, 753093, 753480, 754515, 754844, 754909, 755098
factor Xa
-
mature enzyme
fX
-
-
FXa
-
-
FXa
-
-
649955, 650164, 650846, 650933, 650939, 652262, 652731, 652755, 653979, 683235, 683241, 683243, 683250, 683295, 683443, 683629, 683823, 707279, 707903, 708451, 708505, 708634, 709434, 709578, 717335, 717339, 717381, 717829, 717968, 717974, 718415, 731276, 731308, 731484, 731588, 731756, 731958, 732229, 732937, 752707, 753093, 753480, 754844, 755098
prothrombin activator
-
prothrombinase
-
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prothrombinase
-
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enzyme complex consisting of factor Xa and factor Va, assembled in a calcium-dependent manner on the surface of phospholipid membranes
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prothrombinase
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complex consisting of factor Xa and Va
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
FXa belongs to the family of trypsin-like serine proteases
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
additional information
-
the enzyme belongs to the peptidase family S1, i.e. trypsin family
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selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
649797, 649955, 649987, 650111, 650170, 650179, 650193, 650463, 650846, 650914, 650933, 650938, 650939, 651189, 651191, 652253, 652278, 652349, 652447, 652501, 652731, 652755, 653059, 653400, 653979, 653986
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity, autolysis loop is formed by residues Arg143, Lys147, Arg150, and Arg154
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity, catalytic mechanism
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity, catalytic residues are Ser195 and His57, mechanism
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity, hydrolyzes two petide bonds in prothrombin having (Glu/Asp)-Gly-Arg-(Thr/Ile) as P3-P2-P1-P1' residues, glycine is not the best P2-residue, phenylalanine shows even higher activity at this position
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity, most selective P'2-position, less selective P'1-position, and non-selective P'3-position
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
scutelarin has similar specificity, Ser89 is critical for enzyme activity
-
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
residues His57, Asp102, and Ser195 form the catalytic triad at the active site cleft between the two subdomains
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin
A blood coagulation factor formed from the proenzyme factor X by limited proteolysis. Factor X is a glycoprotein composed of a heavy chain and a light chain, which are generated from a precursor protein by the excision of the tripeptide RKR and held together by one or more disulfide bonds. The activated factor Xa converts prothrombin to thrombin in the presence of factor Va, Ca2+ and phospholipids. Scutelarin (EC 3.4.21.60) has similar specificity, but does not require factor Va.
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2-aminobenzoyl-VQFRILGDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + ILGDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-VQFRSAGDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + SAGDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-VQFRSLEDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + SLEDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-VQFRSLTDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + SLTDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-VQFRSVGDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + SCGDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-VQFRTLGDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + TLGDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
Abz-VMIAALPRTMFIQ-ED-dinitrophenyl + H2O
?
-
-
-
?
activated factor VIII + H2O
factor VIII
apomyoglobin + H2O
?
-
maleylated sperm whale apomyoglobin. Hydrolysed at the Arg31-Leu32 bond
-
-
?
Arg-Gly-Arg-4-nitroanilide + H2O
Arg-Gly-Arg + 4-nitroaniline
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg-4-nitroanilide + N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide + H2O
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg + N-benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
benzoyl-Ile-Glu(gamma-OR)-Gly-Arg-4-nitroanilide + H2O
benzoyl-Ile-Glu(gamma-OR)-Gly-Arg + 4-nitroaniline
-
-
-
?
benzoyl-Ile-Glu(piperidineamide)-Gly-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
benzoyl-Ile-Glu-(-H/OMe)-Gly-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
Boc-L-Asp(OBzl)-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
Boc-L-Asp(OBzl)-L-Pro-L-Arg + 7-amino-4-methylcoumarin
chymotrypsin + H2O
?
-
poor substrate
-
-
?
chymotrypsinogen + H2O
?
-
maleylated and performate-oxidized bovine chymotrypsinogen A is hydrolyzed at the Arg230-Val231 bond and at the Arg15-Ile16 bond
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?
D-cyclohexyl-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
D-cyclohexyl-Gly-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
D-hexahydrotyrosol-L-Ala-L-Arg-4-nitroanilide + H2O
D-hexahydrotyrosol-L-Ala-L-Arg + 4-nitroaniline
-
-
-
-
?
D-hexahydrotyrosyl-L-alanyl-L-arginine-4-nitroanilide + H2O
D-hexahydrotyrosyl-L-alanyl-L-arginine + 4-nitroaniline
-
synthetic chromogenic substrate
-
?
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
synthetic substrate S2238
-
-
?
D-phenylalanyl-L-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-L-pipecolyl-L-arginine + 4-nitroaniline
-
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-
-
?
dimethylsulfonyl-D-norleucine-Gly-Arg-4-nitroanilide + H2O
dimethylsulfonyl-D-norleucine-Gly-Arg + 4-nitroaniline
-
-
-
?
factor VII + H2O
?
-
cleavage of two bonds, rapid cleavage of an Arg-Ile bond and slower cleavage of an Y-Gly bond
-
-
?
factor VIII + H2O
?
-
factor Xa proteolytically activates Factor VIII by cleaving P1 residues Arg372, Arg740, and Arg1689. Factor Xa also catalyzes inactivating cleavages that occur on a slower time scale than the activating ones
-
-
?
factor VIII + H2O
activated factor VIII + B domain
factor X + H2O
?
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cleavage of three bonds
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-
?
FPR-prothrombin + H2O
meizothrombin
-
i.e. prothrombin specifically active site-labeled with D-Phe-Pro-Arg-CH2Cl is cleaved by prothrombinase to intermediate meizothrombin, but the reaction is then directed to formation of a different FPR-prothrombin 2 intermediate product
-
-
?
FPR-prothrombin + H2O
meizothrombin + ?
-
i.e. prothrombin specifically active site-labeled with D-Phe-Pro-Arg-CH2Cl and AF660-labeled, is cleaved by prothrombinase to intermediate meizothrombin, but the reaction is then directed to formation of a different FPR-prothrombin 2 intermediate product
-
-
?
fragment 1.2:prethrombin-2 + H2O
thrombin
-
intermediate of prothrombin processing to thrombin, cleavage site is Arg320
-
?
GPRFFL + H2O
GPR + FFL
-
best substrate
-
?
L-Arg-Gly-Arg-4-nitroanilide + H2O
L-Arg-Gly-Arg + 4-nitroaniline
L-Arg-Gly-L-Arg-4-nitroanilide + H2O
L-Arg-Gly-L-Arg + 4-nitroaniline
meizothrombin + H2O
thrombin
-
intermediate of prothrombin processing to thrombin, cleavage site is Arg271
-
?
methoxycarbonyl-D-cyclohexylglycyl-Gly-L-Arg-4-nitroanilide + H2O
methoxycarbonyl-D-cyclohexylglycyl-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
methoxycarbonyl-D-cyclohexylglycyl-glycyl-L-ariginine-4-nitroanilide + H2O
methoxycarbonyl-D-cyclohexylglycyl-glycyl-L-ariginine + 4-nitroaniline
-
i.e. Spectrozyme fXa, SpfXa
-
?
methoxycarbonylcyclohexyl-Gly-Gly-L-Arg-4-nitroanilide + H2O
methoxycarbonylcyclohexyl-Gly-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
N-2-benzyloxycarbonyl-D-arginyl-L-arginine-4-nitroanilide + H2O
N-2-benzyloxycarbonyl-D-arginyl-L-arginine + 4-nitroaniline
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + 4-nitroaniline
N-alpha-benzyloxycarbonyl-Ile-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Ile-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-benzoyl-Arg-4-nitroanilide + H2O
N-benzoyl-Arg + 4-nitroaniline
-
-
-
?
N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide + H2O
N-benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
-
-
-
?
N6-CBZ-D-Lys-L-Pro-L-Arg-4-nitroanilide + H2O
N6-CBZ-D-Lys-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys-4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + 4-nitrophenol
-
-
-
-
?
prethrombin 1 + H2O
thrombin + ?
-
activation of prethrombin 1 is slow with cleavages at residues R320 and R271 occuring with similar rates
-
-
?
prethrombin-1 + H2O
thrombin + ?
-
-
-
-
?
prethrombin-2 + H2O
thrombin-2
-
smallest zymogen form of thrombin containing only the factor Xa cleavage site 2
-
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
prothrombin + H2O
thrombin + ?
prothrombin + H2O
thrombin + activation peptide
-
-
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
prothrombin + H2O
thrombin + thrombin N-terminal fragment F12
-
at the physiological concentration of prothrombin, thrombin formation results in rapid release of the product into solution due to weak interaction between thrombin and the cleaved N-terminal F12 domain, of which fragment F1 plays an essential role in membrane binding. Thrombin itself interacts with poor affinity with the F12 domain
-
-
?
prothrombin + H2O
thrombin + thrombin propeptide
-
-
-
-
?
prothrombin + H2O
trhombin + ?
ProTS195A + H2O
?
-
the mutant protein also acts as competitive inhibitor of prothrombin activation
-
-
?
recombinant prothrombin R155A/R284A/R271A mutant rMZ-II + H2O
meizothrombin
-
cleavage site is Arg320
reaction intermediate in the reaction with wild-type prothrombin
?
recombinant prothrombin R155A/R284A/R271A/S525C mutant rMZ-II-F + H2O
meizothrombin
-
labeled with fluorescein at Cys525, cleavage site is Arg320
reaction intermediate in the reaction with wild-type prothrombin
?
recombinant prothrombin R155A/R284A/R320A mutant rP2-II + H2O
fragment 1.2:prethrombin-2
-
cleavage site is Arg271
reaction intermediate in the reaction with wild-type prothrombin
?
recombinant prothrombin S525C mutant + H2O
thrombin
-
labeled with fluorescein at Cys525, cleavage sites are Arg271 and Arg320
-
?
S-2765 + H2O
Z-D-Arg-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-glycyl-prolyl-D-arginine-4-nitroanilide + H2O
tosyl-glycyl-prolyl-D-arginine + 4-nitroaniline
-
i.e. Chz-TH, synthetic chromogenic substrate
-
?
Trypsinogen + H2O
?
-
maleylated performate-oxidized trypsinogen, slowly hydrolyzed at the Arg117-Val118 bond
-
-
?
Z-D-Arg-Gly-Arg-4-nitroanilide + H2O
Z-D-Arg-Gly-Arg + 4-nitroaniline
Z-D-Arg-Gly-L-Arg-4-nitroanilide + H2O
Z-D-Arg-Gly-L-Arg + 4-nitroaniline
additional information
?
-
activated factor VIII + H2O
factor VIII
-
proteolytic inactivation
-
-
?
activated factor VIII + H2O
factor VIII
-
inactivation by cleavage at Arg336 and Lys36 of domain A1, low activity
-
-
?
Arg-Gly-Arg-4-nitroanilide + H2O
Arg-Gly-Arg + 4-nitroaniline
-
-
-
-
?
Arg-Gly-Arg-4-nitroanilide + H2O
Arg-Gly-Arg + 4-nitroaniline
-
synthetic substrate S2765
-
-
?
Arg-Gly-Arg-4-nitroanilide + H2O
Arg-Gly-Arg + 4-nitroaniline
-
-
-
-
?
Arg-Gly-Arg-4-nitroanilide + H2O
Arg-G
3.4.21.6 coagulation factor Xa
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